Recombinant Mouse Transthyretin (TTR) Protein (GST)

Name: Recombinant Mouse Transthyretin (TTR) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02229P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Transthyretin (TTR) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P07309
Target Symbol	TTR
Synonyms	Ttr; Transthyretin; Prealbumin
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	AGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTSEGSWEPFASGKTAESGELHGLTTDEKFVEGVYRVELDTKSYWKTLGISPFHEFADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN
Expression Range	23-147aa
Protein Length	Partial
Mol. Weight	40.5kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
Subcellular Location	Secreted.
Protein Families	Transthyretin family
Database References	KEGG: mmu:22139 STRING: 10090.ENSMUSP00000074783 UniGene: PMID: 29360446 Results indicate that TTR stability is important for its recently described functions in assisting Abeta transport at the BBB and at the liver and also in regulating LRP1 levels and activity. TTR stabilization can serve as an avenue to increase both Abeta elimination and LRP1 levels, which in turn will further participate in Abeta clearance. PMID: 28570028 This study reports a possible mechanism for Rhabdomyolysis-Induced Acute Kidney Injury and suggests that reductions in TTR could increase the generation of Reactive Oxygen Species and induce apoptosis. PMID: 29040977 TTR neuritogenic activity is mediated by the megalin receptor and is lost in megalin-deficient neurons. PMID: 27518433 New insights into ghrelin cell physiology, and given the known functions of RBP4 and TTR, support an emerging role for the ghrelin cell in blood glucose handling and metabolism. PMID: 23840311 Transthyretin (TTR) deposition in the peripheral nervous system is the hallmark of familial amyloidotic polyneuropathy (FAP). PMID: 27568093 TTR mediated transport of thyroxine represents a survival mechanism necessary for the myogenic program. PMID: 28075349 provide evidence of a new role of Transthyretin as a transcription inducer of insulin-like growth factor receptor I in central nervous system, unveiling a new role in neuroprotection PMID: 25084758 data also indicate that it is unlikely that the behaviors seen in Ttr(-/-) mice are related to its function PMID: 24956283 Native transthyretin inhibits all preeclampsia-like features in the humanized mouse model. PMID: 24035612 Transthyretin silencing (TTRkd) significantly reduced myogenin expression. PMID: 23717457 Amyloid fibrils formed by a mutant form of TTR, A25T, activate microglia, leading to the secretion of tumor necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6) and nitric oxide. PMID: 24008733 Hsf-1 affects podocyte markers NPHS1, NPHS2 and WT1 in a transgenic mouse model of TTRVal30Met-related amyloidosis. PMID: 23829269 Fibroblasts endocytose and degrade transthyretin aggregates in transthyretin-related amyloidosis. PMID: 23817086 Increased degradation of 14-3-3zeta in lysosomes in the absence of TTR, increasing autophagy. PMID: 23523922 our data demonstrate that the increased expression of Ttr in ob/ob mice does not cause (but rather attenuates) their phenotypic abnormalities. PMID: 22849972 TTR has an important and nonredundant role in influencing the development of several organs. PMID: 23092911 Results suggest that TTR expressed in pancreatic alpha cells may play important roles in glucose homeostasis via regulating the expression of glucagon. PMID: 23108050 TTR binds to Grp78 at the plasma membrane, is internalized into the beta-cell via a clathrin-dependent pathway, and that this internalization is necessary for the effects of TTR on beta-cell function. PMID: 22183612 the expression of transthyretin and protein kinase Cgamma were increased in the prefrontal cortex but not in the hippocampus of naltrexone-treated mice PMID: 21111029 Cerebrospinal fluid transthyretin contributes to control of neuronal cell death, edema and inflammation which influences the survival of endangered neurons in cerebral ischemia. PMID: 21044072 Results identify transthyretin and Klotho as physiological targets of amyloid precursor protein that are regulated by soluble APPsbeta independent of developmental APP functions. PMID: 20855613 TTR mRNA is dramatically up-regulated in the preimplantation mouse uterus as well as the progesterone-treated ovariectomized mouse uterus. PMID: 20188365 Using transthyretin (TTR) KO mice as a model of augmented NPY levels, we showed that this strain has increased NPY content in the bone, further validating the expression of this neuropeptide by bone cells. PMID: 19954489 Transthyretin is not required for thyroid hormone access to or distribution within the mouse brain. PMID: 12182890 Levels of noradrenaline were significantly increased in the limbic forebrain of TTR-null mice. This report represents the first clear indication that TTR plays a role in behaviour, probably by modulation of the noradrenergic system PMID: 15009661 Mice overexpressing mutant APP have high levels of sAPPalpha & transthyretin & do not develop the tau phosphorylation or neuronal loss characteristic of human AD. Anti-transthyretin antibodies reverse this, showing that transthyretin is neuroprotective. PMID: 15342738 Transthyretin is clearly not produced in the brain parenchyma of wild-type mice nor in transgenic mouse models of Alzheimer's disease. PMID: 16698124 The effect of chronic ethanol treatment on transthyretin expression was analyzed because gamma-PKC mutants do not develop tolerance to chronic ethanol treatment. PMID: 16767509 proliferation and apoptosis in the SVZ neural stem cell niche are differentially affected by the lack of TTR synthesis. PMID: 17574756 Our results strongly suggest that TTR plays a critical role in modulating Abeta deposition in vivo. PMID: 17596449 the absence of transthyretin does not seem to influence the regulation of lipid and glucose metabolism PMID: 17611908 data show that the absence of TTR seems to accelerate the poorer cognitive performance normally associated with aging PMID: 17698379 TTR participates in nerve physiology and enhances nerve regeneration PMID: 17897357 Lowering TTR levels or interfering with retinol binding protein 4-TTR binding may enhance insulin sensitivity in obesity and type 2 diabetes PMID: 18285525 TCDD can induce memory deficits by altering the estrogen pathways and a main route of TTR-mediated retinol transport. PMID: 18294692 In mouse DRG, TTR mRNA was localized in the peripheral glial cells. PMID: 18406527 Data show that the degree of total and vascular Abeta burdens in the aged Tg2576/TTR(-/-) mice is significantly reduced relative to the age-matched Tg2576/TTR(+/-) mice. PMID: 18429966 TTR deposited in peripheral nervous system of familial amyloiditic polyneuropathy should be regarded as having blood or CSF origin PMID: 18835560 Results suggest that transthyretin is up-regulated by estradiol via a pathway involving estrogen receptors alpha and beta. PMID: 19130215 TTR has natural substrates in the nervous system PMID: 19138167 Transthyretin, a gene previously suggested to play a role in the reduction of Alzheimer disease, has been identified as a leftward gene asymmetrically expressed in the brains of adult male mice. PMID: 19167467 Axonal retrograde transport is impaired in transthyretin knock-out mice, in addition to neurite outgrowth impairment. PMID: 19279259 Using both GFP-based and LacZ-based Cre reporter strains, we demonstrate that in Ttr::Cre transgenics, Cre-mediated recombination occurs throughout the visceral endoderm PMID: 19415627 he alleged neuroprotective role of TTR in the nervous system should be regarded with caution and should not be generalized to all types of insults PMID: 19595729 rat and murine TTR have a lower intrinsic beta-aggregation propensity and a similar native beta-structure stability compared with human TTR. PMID: 19602727

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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